Ubiquitin-specific peptidase 29 (USP29, MEROPS identifier C19.040) is a de-ubiquitinating enzyme that releases poly-ubiquitin from conjugates. The USP29 gene is activated by a the far upstream element binding protein (FBP) and JTV1, a subunit of the multi-aminoacyl-tRNA synthetase complex. USP29 is then able to stabilize p53 by removing ubiquitin, and accumulated p53 induces apoptosis []. USP29 is also important in the maintenance of genomic integrity because it de-ubiquitinates claspin. Ubiquitinated claspin is degraded by the proteasome, and upregulation of USP29 promotes claspin survival, whereas downregulation promotes claspin degradation []. USP29 knockdown also leads to impaired phosphorylation of Chk1 following DNA damage and cells show a major defect in S-phase progression []. USP29 is paternally imprinted in the mouse [], and conserved sequence element 1 (CSE-1) within the CpG island that surrounds the genes acts as a repressor for transcription of both the USP29 and PEG3 genes [].
This pleckstrin homology (PH)-like domain can be found at the N terminus of some ubiquitin carboxyl-terminal hydrolases, including USP26, USP29 and USP37. USP37 antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), resulting in promoting S phase entry []. USP26 is a regulator of androgen receptor (AR) signaling []. Both USP26 and USP37 are critical for double-strand breaks repair by homologous recombination []. USP29 plays a role in apoptosis and oxidative stress [].PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized.
This entry represents a pleckstrin homology (PH)-like domain found at the N terminus of some ubiquitin carboxyl-terminal hydrolases, including USP26, USP29 and USP37. USP37 antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), resulting in promoting S phase entry []. USP26 is a regulator of androgen receptor (AR) signaling []. Both USP26 and USP37 are critical for double-strand breaks repair by homologous recombination []. USP29 plays a role in apoptosis and oxidative stress [].PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized.
